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Reviewed, UniProtKB/Swiss-Prot O49886 (CYPH_LUPLU)

Last modified June 16, 2009. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peptidyl-prolyl cis-trans isomerase
      Short name=PPIase
      Short name=Rotamase
    EC=5.2.1.8
Alternative name(s):
    Cyclophilin
    Cyclosporin A-binding protein
OrganismLupinus luteus (European yellow lupin)
Taxonomic identifier3873 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IFabalesFabaceaePapilionoideaeGenisteaeLupinus

Protein attributes

Sequence length172 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Catalytic activity

Peptidylproline (omega=180) = peptidylproline (omega=0).

Enzyme regulation

Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase.

Subcellular location

Cytoplasm.

Tissue specificity

Expressed in meristematic tissues, with higher levels in nodules. Ref.1

Sequence similarities

Belongs to the cyclophilin-type PPIase family.

Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandCyclosporin
   Molecular functionIsomerase
Rotamase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionpeptide binding

Inferred from electronic annotation. Source: UniProtKB-KW

peptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 172172Peptidyl-prolyl cis-trans isomerase
PRO_0000064144

Regions

Domain7 – 170164PPIase cyclophilin-type

Secondary structure

................................ 172
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O49886-1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: DD8351276CBEEF1F

FASTA17218,287
        10         20         30         40         50         60 
MSNPKVFFDM AIAGNPAGRI VMELYADTTP RTAENFRALC TGEKGVGRSG KPLHYKGSTF 

        70         80         90        100        110        120 
HRVIPNFMCQ GGDFTAGNGT GAESIYGAKF ADENFIKRHT GPGILSMANA GAGTNGSQFF 

       130        140        150        160        170 
ICTEKTEWLD GKHVVFGKVI EGMNVVRDIE KVGSGSGKTS RPVTIADCGQ LS 

« Hide

References

[1]"Yellow lupine cyclophilin transcripts are highly accumulated in the nodule meristem zone."
Nuc K., Nuc P., Slomski R.
Mol. Plant Microbe Interact. 14:1384-1394(2001) [PubMed: 11768533] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
Strain: cv. Ventus.
Tissue: Seedling.
[2]"Theoretical model of CYPH_LUPLU."
Siddharhta K.
Submitted (AUG-2002) to the PDB data bank
Cited for: 3D-STRUCTURE MODELING.

Cross-references

Sequence databases

Y16088 mRNA. Translation: CAA76054.1.
AF178458 Genomic DNA. Translation: AAF00471.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1MD5model-A1-172[»]
SMRO49886. Positions 1-171.
ModBaseSearch...

Enzyme and pathway databases

BRENDA5.2.1.8. 261.

Family and domain databases

InterProIPR002130. PPIase_cyclophilin.
[Graphical view]
Gene3DG3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSPR00153. CSAPPISMRASE.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYPH_LUPLU
AccessionPrimary (citable) accession number: O49886
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: June 16, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents